GSTF2_ORYSJ
ID GSTF2_ORYSJ Reviewed; 215 AA.
AC O82451; O65858; Q7F5M8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable glutathione S-transferase GSTF2;
DE EC=2.5.1.18;
DE AltName: Full=GST-II;
GN Name=GSTF2; Synonyms=RGST II;
GN OrderedLocusNames=Os01g0764000, LOC_Os01g55830; ORFNames=P0403C05.5;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lemont; TISSUE=Root;
RA Wu J., Cramer C., Hatzios K.K.;
RT "Isolation of a full-length cDNA encoding the second glutathione S-
RT transferase from rice (Oryza sativa).";
RL (er) Plant Gene Register PGR98-136(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP PROTEIN SEQUENCE OF 2-11, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RC TISSUE=Anther, Callus, Panicle, Root, Sheath, and Stem;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-195.
RC STRAIN=cv. Lemont;
RA Wu J., Cramer C., Hatzios K.K.;
RT "Nucleotide sequence of a cDNA encoding the second glutathione S-
RT transferase from rice (Oryza sativa).";
RL (er) Plant Gene Register PGR98-119(1998).
RN [8]
RP CHARACTERIZATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Lemont;
RX DOI=10.1034/j.1399-3054.1999.105116.x;
RA Wu J., Cramer C., Hatzios K.K.;
RT "Characterization of two cDNAs encoding glutathione S-transferases in rice
RT and induction of their transcripts by the herbicide safener fenclorim.";
RL Physiol. Plantarum 105:102-108(1999).
RN [9]
RP NOMENCLATURE, AND INDUCTION.
RX PubMed=15069639; DOI=10.1007/s00438-004-1006-8;
RA Soranzo N., Sari Gorla M., Mizzi L., De Toma G., Frova C.;
RT "Organisation and structural evolution of the rice glutathione S-
RT transferase gene family.";
RL Mol. Genet. Genomics 271:511-521(2004).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots. Expressed in
CC anthers, callus, panicles, sheaths and stems (at protein level).
CC {ECO:0000269|PubMed:14681440, ECO:0000269|Ref.8}.
CC -!- INDUCTION: By the herbicide safener fenclorim. By drought stress.
CC {ECO:0000269|PubMed:15069639, ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF062403; AAC64007.1; -; mRNA.
DR EMBL; AP003239; BAB63585.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74483.1; -; Genomic_DNA.
DR EMBL; AK058894; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK059818; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK099142; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ002381; CAA05355.1; -; mRNA.
DR PIR; T03989; T03989.
DR RefSeq; XP_015614423.1; XM_015758937.1.
DR AlphaFoldDB; O82451; -.
DR SMR; O82451; -.
DR BioGRID; 795924; 1.
DR STRING; 4530.OS01T0764000-01; -.
DR PaxDb; O82451; -.
DR PRIDE; O82451; -.
DR EnsemblPlants; Os01t0764000-01; Os01t0764000-01; Os01g0764000.
DR EnsemblPlants; Os01t0764000-03; Os01t0764000-03; Os01g0764000.
DR GeneID; 4326887; -.
DR Gramene; Os01t0764000-01; Os01t0764000-01; Os01g0764000.
DR Gramene; Os01t0764000-03; Os01t0764000-03; Os01g0764000.
DR KEGG; osa:4326887; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; O82451; -.
DR OMA; FEQELSC; -.
DR OrthoDB; 1231780at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; O82451; baseline and differential.
DR Genevisible; O82451; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03187; GST_C_Phi; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR034347; GST_Phi_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14681440"
FT CHAIN 2..215
FT /note="Probable glutathione S-transferase GSTF2"
FT /id="PRO_0000185845"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 88..215
FT /note="GST C-terminal"
FT BINDING 12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 190
FT /note="H -> Q (in Ref. 7; CAA05355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 23977 MW; F956905A623D07D0 CRC64;
MAPMKLYGST LSWNVTRCVA VLEEAGAEYE IVPLDFSKGE HKAPDHLARN PFGQVPALQD
GDLFLWESRA ICKYVCRKNK PELLKDGDLK ESAMVDVWLE VESNQYTPAL NPILFQCLIR
PMMFGAPPDE KVVEENLEKL KKVLEVYEAR LTKCKYLAGD YISVADLSHV AGTVCLGATP
HASVLDAYPH VKAWWTDLMA RPSSQKVASL MKPPA
